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Conserved domains on  [gi|515134243|ref|WP_016763034|]
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UDP-glucose--hexose-1-phosphate uridylyltransferase [Priestia megaterium]

Protein Classification

UDP-glucose--hexose-1-phosphate uridylyltransferase( domain architecture ID 11468239)

UDP-glucose--hexose-1-phosphate uridylyltransferase catalyzes the conversion from UDP-alpha-D-glucose and alpha-D-galactose 1-phosphate to alpha-D-glucose 1-phosphate and UDP-alpha-D-galactose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GalT2 COG4468
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
4-504 0e+00

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 443565  Cd Length: 499  Bit Score: 914.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   4 NIHEEITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLDECIIVEVKEERLEHPAAILDNMLDWAAENNRIaENSITYRDL 83
Cdd:COG4468    2 MINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEENEESLPEILDELLDYAVENGLI-EDTVTERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  84 FDTKIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKA 163
Cdd:COG4468   81 FDTKIMGLLTPRPSEVNRKFWELYAESPKAATDYFYKLSKDSNYIRTDRIAKNIKWKTPTEYGDLEITINLSKPEKDPKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 164 IAASKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFK 243
Cdd:COG4468  161 IAAAKNAKQSSYPKCLLCKENEGYAGRLNHPARQNHRIIPLTLNGEDWGFQYSPYVYYNEHCIVLSEEHRPMKIDRATFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 244 RLLAFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTP 323
Cdd:COG4468  241 RLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTFPMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSEDKER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 324 LVEAADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIG 403
Cdd:COG4468  321 LVEAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKKENIG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 404 LIEVMGLAVLPGRLKDEMSLVAKGLVQNNLNELASrhDQVQKHVKWAEQIEKKYPHIEEQNVQSILQQELGLVFATILEH 483
Cdd:COG4468  401 LIEVMGLAVLPGRLKEELEEVKKYLLGEKKDIEEN--EVLAKHAEWAEELKAKYPTLTKENVEEILKEEVGKVFERVLED 478
                        490       500
                 ....*....|....*....|.
gi 515134243 484 AGVFKQNTEGQLAFSRFMNSL 504
Cdd:COG4468  479 AGVFKRDEEGRAAFKRFIESL 499
 
Name Accession Description Interval E-value
GalT2 COG4468
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
4-504 0e+00

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 443565  Cd Length: 499  Bit Score: 914.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   4 NIHEEITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLDECIIVEVKEERLEHPAAILDNMLDWAAENNRIaENSITYRDL 83
Cdd:COG4468    2 MINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEENEESLPEILDELLDYAVENGLI-EDTVTERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  84 FDTKIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKA 163
Cdd:COG4468   81 FDTKIMGLLTPRPSEVNRKFWELYAESPKAATDYFYKLSKDSNYIRTDRIAKNIKWKTPTEYGDLEITINLSKPEKDPKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 164 IAASKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFK 243
Cdd:COG4468  161 IAAAKNAKQSSYPKCLLCKENEGYAGRLNHPARQNHRIIPLTLNGEDWGFQYSPYVYYNEHCIVLSEEHRPMKIDRATFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 244 RLLAFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTP 323
Cdd:COG4468  241 RLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTFPMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSEDKER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 324 LVEAADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIG 403
Cdd:COG4468  321 LVEAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKKENIG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 404 LIEVMGLAVLPGRLKDEMSLVAKGLVQNNLNELASrhDQVQKHVKWAEQIEKKYPHIEEQNVQSILQQELGLVFATILEH 483
Cdd:COG4468  401 LIEVMGLAVLPGRLKEELEEVKKYLLGEKKDIEEN--EVLAKHAEWAEELKAKYPTLTKENVEEILKEEVGKVFERVLED 478
                        490       500
                 ....*....|....*....|.
gi 515134243 484 AGVFKQNTEGQLAFSRFMNSL 504
Cdd:COG4468  479 AGVFKRDEEGRAAFKRFIESL 499
PRK05270 PRK05270
UDP-glucose--hexose-1-phosphate uridylyltransferase;
4-504 0e+00

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 235382 [Multi-domain]  Cd Length: 493  Bit Score: 872.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   4 NIHEEITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLDEcIIVEVKEERLEHPAAILDNMLDWAAENNRIaENSITYRDL 83
Cdd:PRK05270   2 TISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDS-YEEVDEDEDLESPIDLLDQLVDYAVENGLI-EDTQTERDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  84 FDTKIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKA 163
Cdd:PRK05270  80 LDAQLMDLLTPRPSEVNRRFWEKYQKSPEAATDYFYQLSKANNYIKTDAIAKNISWKVPTKYGDLEITINLSKPEKDPKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 164 IAASKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFK 243
Cdd:PRK05270 160 IAAAKKAKASSYPKCLLCMENEGYAGRLNHPARSNHRIIRLTLGGESWGFQYSPYAYFNEHCIVLSEKHRPMKISRKTFE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 244 RLLAFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTP 323
Cdd:PRK05270 240 RLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFPMAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKDE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 324 LVEAADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIG 403
Cdd:PRK05270 320 LIDAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENIG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 404 LIEVMGLAVLPGRLKDEMSLVAKGLVQNNlNELAsrhdqvQKHVKWAEQIEKKYPHIEEQNVQSILQQELGLVFATILEH 483
Cdd:PRK05270 400 LIEVMGLAILPGRLKEELEEVEKYLLGEA-NEVA------AKHQEWAEQLKAKYGITTKENVEAIVQEEVGSVFARVLED 472
                        490       500
                 ....*....|....*....|.
gi 515134243 484 AGVFKQNTEGQLAFSRFMNSL 504
Cdd:PRK05270 473 AGVFKRTEEGQAAFDRFIESL 493
galT_2 TIGR01239
galactose-1-phosphate uridylyltransferase, family 2; This enzyme is involved in glucose and ...
9-504 0e+00

galactose-1-phosphate uridylyltransferase, family 2; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087 from Pfam. [Energy metabolism, Sugars]


Pssm-ID: 273519  Cd Length: 489  Bit Score: 661.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243    9 ITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLdECIIVEVKEERLEHPAA--ILDNMLDWAAENNRIAENsITYRDLFDT 86
Cdd:TIGR01239   2 VNQFIEYALENGDIEILDREYLRNRLLEALGI-THPDENSSTSILQNQSSpdLLDQLLQWAAENGRMEAD-TTQRDILEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   87 KIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKAIAA 166
Cdd:TIGR01239  80 KLMDLITPRPSEVNRKFWETYASYPEQATKYFYQYSKRVYYVKTDAIAKNIHYTVPTEYGDLEITINLSKPEKDPKAIAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  167 SKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFKRLL 246
Cdd:TIGR01239 160 AKEAKQSSYPACQLCMENEGFEGSVNHPARSNHRIIRVILEDEQWGFQFSPYAYFPEHSIVLKGKHEPMEISKKTFERLL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  247 AFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTPLVE 326
Cdd:TIGR01239 240 SFLGKFPHYFIGSNADLPIVGGSILSHDHYQGGRHDFPMARAEAEEVYELNDYPDVSAGIVKWPMSVLRLQGEDPGELAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  327 AADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIGLIE 406
Cdd:TIGR01239 320 AADHIFRTWQTYSDEKAGIAAYSDGTPHHTVTPIARRRDGKYELDLVLRDNQTSEEYPDGIFHPHQDVHHIKKENIGLIE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  407 VMGLAVLPGRLKDEMSLVAKGLVqNNLNELASrhdqvqKHVKWAEQIEKKYpHIEEQNVQSILQQELGLVFATILEHAGV 486
Cdd:TIGR01239 400 VMGLAILPGRLKTELKEVEAYLL-GQDNQLTA------IHKEWADRLKEKR-NITKENVDLVIKQEVGHVFARVLEDAGV 471
                         490
                  ....*....|....*...
gi 515134243  487 FKQNTEGQLAFSRFMNSL 504
Cdd:TIGR01239 472 FKQTAEGKQGFRKFIDFL 489
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
21-234 1.07e-44

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 155.14  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   21 LLTKWDIDVVRN-KLLEVLKLDeciiVEVKEERLEHPaaildnmldWAAENNRIAENSITYRDLfdtkiMGCFASMPSEV 99
Cdd:pfam01087   1 LFEETDHIYLSHrRYNPLTGEW----VLVSPHRLKRP---------WAGQQEKISKDTLPEYDP-----MCYLCPGPSRA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  100 NRTFYEHYQqSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPE--------KDPKAIAAS---- 167
Cdd:pfam01087  63 NGDFNPDYK-SPFVFTNDFYALSKDNPYIKTDAIAKNILFKAETVYGDCEVTCFLSKPEltlplmspKDPKAIAAAwqek 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  168 -KSLKESNYPLCLLCKENAGYAGRIN--HParqnhriipvelqeelwymqfspyvyyneHAIVFASEHTP 234
Cdd:pfam01087 142 yAELGASSYPKCVLCFENEGYAMGCSnpHP-----------------------------HGQIWASSHLP 182
 
Name Accession Description Interval E-value
GalT2 COG4468
Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];
4-504 0e+00

Galactose-1-phosphate uridylyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 443565  Cd Length: 499  Bit Score: 914.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   4 NIHEEITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLDECIIVEVKEERLEHPAAILDNMLDWAAENNRIaENSITYRDL 83
Cdd:COG4468    2 MINQAIERLVEYAIKNGLIEEEDRIYARNRLLELLGLDEPEEPEVEEENEESLPEILDELLDYAVENGLI-EDTVTERDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  84 FDTKIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKA 163
Cdd:COG4468   81 FDTKIMGLLTPRPSEVNRKFWELYAESPKAATDYFYKLSKDSNYIRTDRIAKNIKWKTPTEYGDLEITINLSKPEKDPKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 164 IAASKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFK 243
Cdd:COG4468  161 IAAAKNAKQSSYPKCLLCKENEGYAGRLNHPARQNHRIIPLTLNGEDWGFQYSPYVYYNEHCIVLSEEHRPMKIDRATFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 244 RLLAFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTP 323
Cdd:COG4468  241 RLLDFVEQFPHYFIGSNADLPIVGGSILSHDHFQGGRYTFPMEKAPIEEEFTLKGFPDVEAGIVKWPMSVIRLRSEDKER 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 324 LVEAADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIG 403
Cdd:COG4468  321 LVEAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPLGIFHPHAEVHHIKKENIG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 404 LIEVMGLAVLPGRLKDEMSLVAKGLVQNNLNELASrhDQVQKHVKWAEQIEKKYPHIEEQNVQSILQQELGLVFATILEH 483
Cdd:COG4468  401 LIEVMGLAVLPGRLKEELEEVKKYLLGEKKDIEEN--EVLAKHAEWAEELKAKYPTLTKENVEEILKEEVGKVFERVLED 478
                        490       500
                 ....*....|....*....|.
gi 515134243 484 AGVFKQNTEGQLAFSRFMNSL 504
Cdd:COG4468  479 AGVFKRDEEGRAAFKRFIESL 499
PRK05270 PRK05270
UDP-glucose--hexose-1-phosphate uridylyltransferase;
4-504 0e+00

UDP-glucose--hexose-1-phosphate uridylyltransferase;


Pssm-ID: 235382 [Multi-domain]  Cd Length: 493  Bit Score: 872.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   4 NIHEEITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLDEcIIVEVKEERLEHPAAILDNMLDWAAENNRIaENSITYRDL 83
Cdd:PRK05270   2 TISQLIEKLIDYAIQNGLIEELDRIYLRNRLLALLGEDS-YEEVDEDEDLESPIDLLDQLVDYAVENGLI-EDTQTERDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  84 FDTKIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKA 163
Cdd:PRK05270  80 LDAQLMDLLTPRPSEVNRRFWEKYQKSPEAATDYFYQLSKANNYIKTDAIAKNISWKVPTKYGDLEITINLSKPEKDPKA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 164 IAASKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFK 243
Cdd:PRK05270 160 IAAAKKAKASSYPKCLLCMENEGYAGRLNHPARSNHRIIRLTLGGESWGFQYSPYAYFNEHCIVLSEKHRPMKISRKTFE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 244 RLLAFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTP 323
Cdd:PRK05270 240 RLLDFVEQFPHYFIGSNADLPIVGGSILSHDHYQGGRHTFPMAKAPIEEEFTLAGYPDVKAGIVKWPMSVIRLTSKNKDE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 324 LVEAADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIG 403
Cdd:PRK05270 320 LIDAADKILEAWRGYSDESVDILAYTDGTPHNTITPIARRRGGKYELDLVLRNNRTSEEHPDGIFHPHPEVHHIKKENIG 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243 404 LIEVMGLAVLPGRLKDEMSLVAKGLVQNNlNELAsrhdqvQKHVKWAEQIEKKYPHIEEQNVQSILQQELGLVFATILEH 483
Cdd:PRK05270 400 LIEVMGLAILPGRLKEELEEVEKYLLGEA-NEVA------AKHQEWAEQLKAKYGITTKENVEAIVQEEVGSVFARVLED 472
                        490       500
                 ....*....|....*....|.
gi 515134243 484 AGVFKQNTEGQLAFSRFMNSL 504
Cdd:PRK05270 473 AGVFKRTEEGQAAFDRFIESL 493
galT_2 TIGR01239
galactose-1-phosphate uridylyltransferase, family 2; This enzyme is involved in glucose and ...
9-504 0e+00

galactose-1-phosphate uridylyltransferase, family 2; This enzyme is involved in glucose and galactose interconversion. This model describes one of two extremely distantly related branches of the model pfam01087 from Pfam. [Energy metabolism, Sugars]


Pssm-ID: 273519  Cd Length: 489  Bit Score: 661.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243    9 ITRLIQYGLQKNLLTKWDIDVVRNKLLEVLKLdECIIVEVKEERLEHPAA--ILDNMLDWAAENNRIAENsITYRDLFDT 86
Cdd:TIGR01239   2 VNQFIEYALENGDIEILDREYLRNRLLEALGI-THPDENSSTSILQNQSSpdLLDQLLQWAAENGRMEAD-TTQRDILEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   87 KIMGCFASMPSEVNRTFYEHYQQSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPEKDPKAIAA 166
Cdd:TIGR01239  80 KLMDLITPRPSEVNRKFWETYASYPEQATKYFYQYSKRVYYVKTDAIAKNIHYTVPTEYGDLEITINLSKPEKDPKAIAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  167 SKSLKESNYPLCLLCKENAGYAGRINHPARQNHRIIPVELQEELWYMQFSPYVYYNEHAIVFASEHTPMHISKQTFKRLL 246
Cdd:TIGR01239 160 AKEAKQSSYPACQLCMENEGFEGSVNHPARSNHRIIRVILEDEQWGFQFSPYAYFPEHSIVLKGKHEPMEISKKTFERLL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  247 AFVEQFPHYFLGSNADLPIVGGSILTHDHFQGGYHDFPMAKAKINKLFSLKAYPDVKAGIVHWPMSVVRLQSSHLTPLVE 326
Cdd:TIGR01239 240 SFLGKFPHYFIGSNADLPIVGGSILSHDHYQGGRHDFPMARAEAEEVYELNDYPDVSAGIVKWPMSVLRLQGEDPGELAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  327 AADFILKKWKSYSDQSADILAFTDQTPHNTVTPIARKRGDLYELDLVLRNNRTNGKHPGGIYHPHAEVHHIKKENIGLIE 406
Cdd:TIGR01239 320 AADHIFRTWQTYSDEKAGIAAYSDGTPHHTVTPIARRRDGKYELDLVLRDNQTSEEYPDGIFHPHQDVHHIKKENIGLIE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  407 VMGLAVLPGRLKDEMSLVAKGLVqNNLNELASrhdqvqKHVKWAEQIEKKYpHIEEQNVQSILQQELGLVFATILEHAGV 486
Cdd:TIGR01239 400 VMGLAILPGRLKTELKEVEAYLL-GQDNQLTA------IHKEWADRLKEKR-NITKENVDLVIKQEVGHVFARVLEDAGV 471
                         490
                  ....*....|....*...
gi 515134243  487 FKQNTEGQLAFSRFMNSL 504
Cdd:TIGR01239 472 FKQTAEGKQGFRKFIDFL 489
GalP_UDP_transf pfam01087
Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication ...
21-234 1.07e-44

Galactose-1-phosphate uridyl transferase, N-terminal domain; SCOP reports fold duplication with C-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 426039 [Multi-domain]  Cd Length: 182  Bit Score: 155.14  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243   21 LLTKWDIDVVRN-KLLEVLKLDeciiVEVKEERLEHPaaildnmldWAAENNRIAENSITYRDLfdtkiMGCFASMPSEV 99
Cdd:pfam01087   1 LFEETDHIYLSHrRYNPLTGEW----VLVSPHRLKRP---------WAGQQEKISKDTLPEYDP-----MCYLCPGPSRA 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  100 NRTFYEHYQqSPQKATSYYYKLSKDIHYIRRDRIAKNERWVTNTDFGELEITINLSKPE--------KDPKAIAAS---- 167
Cdd:pfam01087  63 NGDFNPDYK-SPFVFTNDFYALSKDNPYIKTDAIAKNILFKAETVYGDCEVTCFLSKPEltlplmspKDPKAIAAAwqek 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  168 -KSLKESNYPLCLLCKENAGYAGRIN--HParqnhriipvelqeelwymqfspyvyyneHAIVFASEHTP 234
Cdd:pfam01087 142 yAELGASSYPKCVLCFENEGYAMGCSnpHP-----------------------------HGQIWASSHLP 182
GalP_UDP_tr_C pfam02744
Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication ...
249-440 2.64e-29

Galactose-1-phosphate uridyl transferase, C-terminal domain; SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.


Pssm-ID: 397044 [Multi-domain]  Cd Length: 166  Bit Score: 112.96  E-value: 2.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  249 VEQFPHYFLGSnadlpivgGSILTHDHFQggyhdfpMAKAKINKLFSLK-AYPDVKAGIVHWPMSVVRLQSSHLTPLVEA 327
Cdd:pfam02744   2 LRSFPKYFAGH--------GSILLHDYVQ-------MELAEKERVVVENeSWPVVVPYWAKWPFETLLLPKRHVPSLTEL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515134243  328 ADfilkkwksysDQSADILAftdqtphnTVTPIARKRGDLYEldlvlrnnrTNGKHPGGI--------------YHPHAE 393
Cdd:pfam02744  67 TD----------AEREDLAA--------ILKPLTRRYDNLFE---------TSFPYSMGIhqaplnaeelnhwqFHPHFY 119
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 515134243  394 VHHIKKENIGLIEVmGLAVLPGRLKDEMSLVAKGLvqnnLNELASRH 440
Cdd:pfam02744 120 PPLLRSATVRKFMV-GLEILGERQRDLTAEQAAER----LRALSEVH 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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